Science 24 February 1989: Vol. 243. no. 4894, pp. 1074 - 1076 DOI: 10.1126/science.2466334

Prev | Table of Contents | Next

Articles

The Kinetics of the Hydrogen/Deuterium Exchange of Epidermal Growth Factor Receptor Ligands.

I. Iloro, D. Narvaez, N. Guillen, C. M. Camacho, L. Guillen, E. Cora, and B. Pastrana-Rios (2008)
Biophys. J. 94, 4041-4055
 |  Abstract »  |  Full Text »  |  PDF »

The Role of Amphiregulin in Exemestane-Resistant Breast Cancer Cells: Evidence of an Autocrine Loop.

X. Wang, S. Masri, S. Phung, and S. Chen (2008)
Cancer Res. 68, 2259-2265
 |  Abstract »  |  Full Text »  |  PDF »

Activation of a Nuclear Factor {kappa}B/Interleukin-1 Positive Feedback Loop by Amphiregulin in Human Breast Cancer Cells.

K. L. Streicher, N. E. Willmarth, J. Garcia, J. L. Boerner, T. G. Dewey, and S. P. Ethier (2007)
Mol. Cancer Res. 5, 847-861
 |  Abstract »  |  Full Text »  |  PDF »

Mitogenic Activity and Signaling Mechanism of 2-(14,15- Epoxyeicosatrienoyl)Glycerol, a Novel Cytochrome P450 Arachidonate Metabolite.

J. Chen, J.-K. Chen, J. R. Falck, S. Anjaiah, J. H. Capdevila, and R. C. Harris (2007)
Mol. Cell. Biol. 27, 3023-3034
 |  Abstract »  |  Full Text »  |  PDF »

Autocrine and Juxtacrine Effects of Amphiregulin on the Proliferative, Invasive, and Migratory Properties of Normal and Neoplastic Human Mammary Epithelial Cells.

N. E. Willmarth and S. P. Ethier (2006)
J. Biol. Chem. 281, 37728-37737
 |  Abstract »  |  Full Text »  |  PDF »

Sialidase fusion protein as a novel broad-spectrum inhibitor of influenza virus infection..

M. P. Malakhov, L. M. Aschenbrenner, D. F. Smee, M. K. Wandersee, R. W. Sidwell, L. V. Gubareva, V. P. Mishin, F. G. Hayden, D. H. Kim, A. Ing, et al. (2006)
Antimicrob. Agents Chemother. 50, 1470-1479
 |  Abstract »  |  Full Text »  |  PDF »

Role of the Epidermal Growth Factor Network in Ovarian Follicles.

M. Conti, M. Hsieh, J.-Y. Park, and Y.-Q. Su (2006)
Mol. Endocrinol. 20, 715-723
 |  Abstract »  |  Full Text »  |  PDF »

Prolactin Potentiates Transforming Growth Factor {alpha} Induction of Mammary Neoplasia in Transgenic Mice.

L. M. Arendt, T. A. Rose-Hellekant, E. P. Sandgren, and L. A. Schuler (2006)
Am. J. Pathol. 168, 1365-1374
 |  Abstract »  |  Full Text »  |  PDF »

Hypoxia induces epithelial amphiregulin gene expression in a CREB-dependent manner.

S. M. O'Reilly, M. O. Leonard, N. Kieran, K. M. Comerford, E. Cummins, M. Pouliot, S. B. Lee, and C. T. Taylor (2006)
Am J Physiol Cell Physiol 290, C592-C600
 |  Abstract »  |  Full Text »  |  PDF »

The Membrane-anchoring Domain of Epidermal Growth Factor Receptor Ligands Dictates Their Ability to Operate in Juxtacrine Mode.

J. Dong, L. K. Opresko, W. Chrisler, G. Orr, R. D. Quesenberry, D. A. Lauffenburger, and H. S. Wiley (2005)
Mol. Biol. Cell 16, 2984-2998
 |  Abstract »  |  Full Text »  |  PDF »

Amphiregulin Is a Novel Growth Factor Involved in Normal Bone Development and in the Cellular Response to Parathyroid Hormone Stimulation.

L. Qin, J. Tamasi, L. Raggatt, X. Li, J. H. M. Feyen, D. C. Lee, E. DiCicco-Bloom, and N. C. Partridge (2005)
J. Biol. Chem. 280, 3974-3981
 |  Abstract »  |  Full Text »  |  PDF »

The Epidermal Growth Factor-Like Growth Factor Amphiregulin Is Strongly Induced by the Adenosine 3',5'-Monophosphate Pathway in Various Cell Types.

C. C. Johansson, A. Yndestad, J. M. Enserink, A. H. Ree, P. Aukrust, and K. Tasken (2004)
Endocrinology 145, 5177-5184
 |  Abstract »  |  Full Text »  |  PDF »

Selective Roles for Tumor Necrosis Factor {alpha}-converting Enzyme/ADAM17 in the Shedding of the Epidermal Growth Factor Receptor Ligand Family: THE JUXTAMEMBRANE STALK DETERMINES CLEAVAGE EFFICIENCY.

C. L. Hinkle, S. W. Sunnarborg, D. Loiselle, C. E. Parker, M. Stevenson, W. E. Russell, and D. C. Lee (2004)
J. Biol. Chem. 279, 24179-24188
 |  Abstract »  |  Full Text »  |  PDF »

Wound-Induced HB-EGF Ectodomain Shedding and EGFR Activation in Corneal Epithelial Cells.

K.-P. Xu, Y. Ding, J. Ling, Z. Dong, and F.-S. X. Yu (2004)
Invest. Ophthalmol. Vis. Sci. 45, 813-820
 |  Abstract »  |  Full Text »  |  PDF »

Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands.

U. Sahin, G. Weskamp, K. Kelly, H.-M. Zhou, S. Higashiyama, J. Peschon, D. Hartmann, P. Saftig, and C. P. Blobel (2004)
J. Cell Biol. 164, 769-779
 |  Abstract »  |  Full Text »  |  PDF »

Amphiregulin Overexpression Results in Rapidly Growing Keratinocytic Tumors: An In Vivo Xenograft Model of Keratoacanthoma.

S. D. Billings, M. D. Southall, T. Li, P. W. Cook, L. Baldridge, W. B. Moores, D. F. Spandau, J. G. Foley, and J. B. Travers (2003)
Am. J. Pathol. 163, 2451-2458
 |  Abstract »  |  Full Text »

Ligand-independent Dimer Formation of Epidermal Growth Factor Receptor (EGFR) Is a Step Separable from Ligand-induced EGFR Signaling.

X. Yu, K. D. Sharma, T. Takahashi, R. Iwamoto, and E. Mekada (2002)
Mol. Biol. Cell 13, 2547-2557
 |  Abstract »  |  Full Text »  |  PDF »

Tumor Necrosis Factor-alpha Converting Enzyme (TACE) Regulates Epidermal Growth Factor Receptor Ligand Availability.

S. W. Sunnarborg, C. L. Hinkle, M. Stevenson, W. E. Russell, C. S. Raska, J. J. Peschon, B. J. Castner, M. J. Gerhart, R. J. Paxton, R. A. Black, et al. (2002)
J. Biol. Chem. 277, 12838-12845
 |  Abstract »  |  Full Text »  |  PDF »

Quantitative analysis of the EGF receptor autocrine system reveals cryptic regulation of cell response by ligand capture.

A. E. DeWitt, J. Y. Dong, H. S. Wiley, and D. A. Lauffenburger (2002)
J. Cell Sci. 114, 2301-2313
 |  Abstract »  |  Full Text »  |  PDF »

Teratogenicity of 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) in Mice Lacking the Expression of EGF and/or TGF-{{alpha}}.

P. L. Bryant, J. E. Schmid, S. E. Fenton, A. R. Buckalew, and B. D. Abbott (2001)
Toxicol. Sci. 62, 103-114
 |  Abstract »  |  Full Text »  |  PDF »

The Egr-1 gene is induced by epidermal growth factor in ECV304 cells and primary endothelial cells.

J. C. Tsai, L. Liu, J. Guan, and W. C. Aird (2000)
Am J Physiol Cell Physiol 279, C1414-C1424
 |  Abstract »  |  Full Text »  |  PDF »

Ectodomain Shedding of Epidermal Growth Factor Receptor Ligands Is Required for Keratinocyte Migration in Cutaneous Wound Healing.

S. Tokumaru, S. Higashiyama, T. Endo, T. Nakagawa, J.-i. Miyagawa, K. Yamamori, Y. Hanakawa, H. Ohmoto, K. Yoshino, Y. Shirakata, et al. (2000)
J. Cell Biol. 151, 209-220
 |  Abstract »  |  Full Text »  |  PDF »

Antisense Inhibition of Epidermal Growth Factor Receptor Decreases Expression of Human Surfactant Protein A.

J. M. Klein, T. A. McCarthy, J. M. Dagle, and J. M. Snyder (2000)
Am. J. Respir. Cell Mol. Biol. 22, 676-684
 |  Abstract »  |  Full Text »

Epiregulin, a Novel Member of the Epidermal Growth Factor Family, Is an Autocrine Growth Factor in Normal Human Keratinocytes.

Y. Shirakata, T. Komurasaki, H. Toyoda, Y. Hanakawa, K. Yamasaki, S. Tokumaru, K. Sayama, and K. Hashimoto (2000)
J. Biol. Chem. 275, 5748-5753
 |  Abstract »  |  Full Text »  |  PDF »

Trafficking and Proteolytic Release of Epidermal Growth Factor Receptor Ligands Are Modulated by Their Membrane-anchoring Domains.

J. Dong and H. S. Wiley (2000)
J. Biol. Chem. 275, 557-564
 |  Abstract »  |  Full Text »  |  PDF »

Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor.

J. Dong, L. K. Opresko, P. J. Dempsey, D. A. Lauffenburger, R. J. Coffey, and H. S. Wiley (1999)
PNAS 96, 6235-6240
 |  Abstract »  |  Full Text »  |  PDF »

A Differential Requirement for the COOH-terminal Region of the Epidermal Growth Factor (EGF) Receptor in Amphiregulin and EGF Mitogenic Signaling.

L. Wong, T. B. Deb, S. A. Thompson, A. Wells, and G. R. Johnson (1999)
J. Biol. Chem. 274, 8900-8909
 |  Abstract »  |  Full Text »  |  PDF »

Targeted inactivation of the EGF and amphiregulin genes reveals distinct roles for EGF receptor ligands in mouse mammary gland development.

N. Luetteke, T. Qiu, S. Fenton, K. Troyer, R. Riedel, A Chang, and D. Lee (1999)
Development 126, 2739-2750
 |  Abstract »  |  PDF »

Heparin-binding EGF-like growth factor interacts with mouse blastocysts independently of ErbB1: a possible role for heparan sulfate proteoglycans and ErbB4 in blastocyst implantation.

B. Paria, K Elenius, M Klagsbrun, and S. Dey (1999)
Development 126, 1997-2005
 |  Abstract »  |  PDF »

Biological Response to ErbB Ligands in Nontransformed Cell Lines Correlates with a Specific Pattern of Receptor Expression.

S. Sundaresan, P. E. Roberts, K. L. King, M. X. Sliwkowski, and J. P. Mather (1998)
Endocrinology 139, 4756-4764
 |  Abstract »  |  Full Text »  |  PDF »

Removal of the Membrane-anchoring Domain of Epidermal Growth Factor Leads to Intracrine Signaling and Disruption of Mammary Epithelial Cell Organization.

H. S. Wiley, M. F. Woolf, L. K. Opresko, P. M. Burke, B. Will, J. R. Morgan, and D. A. Lauffenburger (1998)
J. Cell Biol. 143, 1317-1328
 |  Abstract »  |  Full Text »  |  PDF »

ErbB-1 and ErbB-2 Acquire Distinct Signaling Properties Dependent upon Their Dimerization Partner.

M. A. Olayioye, D. Graus-Porta, R. R. Beerli, J. Rohrer, B. Gay, and N. E. Hynes (1998)
Mol. Cell. Biol. 18, 5042-5051
 |  Abstract »  |  Full Text »

Tyrosine Phosphorylation and Proteolysis. PERVANADATE-INDUCED, METALLOPROTEASE-DEPENDENT CLEAVAGE OF THE ErbB-4 RECEPTOR AND AMPHIREGULIN.

M. Vecchi, L. A. Rudolph-Owen, C. L. Brown, P. J. Dempsey, and G. Carpenter (1998)
J. Biol. Chem. 273, 20589-20595
 |  Abstract »  |  Full Text »  |  PDF »

Cell Surface Ectodomain Cleavage of Human Amphiregulin Precursor Is Sensitive to a Metalloprotease Inhibitor. RELEASE OF A PREDOMINANT N-GLYCOSYLATED 43-kDa SOLUBLE FORM.

C. L. Brown, K. S. Meise, G. D. Plowman, R. J. Coffey, and P. J. Dempsey (1998)
J. Biol. Chem. 273, 17258-17268
 |  Abstract »  |  Full Text »  |  PDF »

Comparative Phenotypic Studies of Duct Epithelial Cell Lines Derived from Normal Human Pancreas and Pancreatic Carcinoma.

N. Liu, T. Furukawa, M. Kobari, and M.-S. Tsao (1998)
Am. J. Pathol. 153, 263-269
 |  Abstract »  |  Full Text »  |  PDF »

ErbB2 expression increases the spectrum and potency of ligand-mediated signal transduction through ErbB4.

L.-M. Wang, A. Kuo, M. Alimandi, M. C. Veri, C.-C. Lee, V. Kapoor, N. Ellmore, X.-H. Chen, and J. H. Pierce (1998)
PNAS 95, 6809-6814
 |  Abstract »  |  Full Text »  |  PDF »

Differential Dose-Dependent Effects of Epidermal Growth Factor on Gene Expression in A431 Cells: Evidence for a Signal Transduction Pathway That Can Bypass Raf-1 Activation.

M. Silvy, P.-M. Martin, N. Chajry, and Y. Berthois (1998)
Endocrinology 139, 2382-2391
 |  Abstract »  |  Full Text »  |  PDF »

Targeted Expression of a Dominant Negative Epidermal Growth Factor Receptor in the Mammary Gland of Transgenic Mice Inhibits Pubertal Mammary Duct Development.

W. Xie, A. J. Paterson, E. Chin, L. M. Nabell, and J. E. Kudlow (1997)
Mol. Endocrinol. 11, 1766-1781
 |  Abstract »  |  Full Text »

Increased expression of transforming growth factor alpha  precursors in acute experimental colitis in rats.

P Hoffmann, J M Zeeh, J Lakshmanan, V S Wu, F Procaccino, M Reinshagen, J A McRoberts, and V E Eysselein (1997)
Gut 41, 195-202
 |  Abstract »  |  Full Text »  |  PDF »

A differential display strategy identifies Cryptic, a novel EGF-related gene expressed in the axial and lateral mesoderm during mouse gastrulation.

M. Shen, H Wang, and P Leder (1997)
Development 124, 429-442
 |  Abstract »  |  PDF »

Amino-terminal Processing of Cell Surface Heparin-binding Epidermal Growth Factor-like Growth Factor Up-regulates Its Juxtacrine but Not Its Paracrine Growth Factor Activity.

T. Nakagawa, S. Higashiyama, T. Mitamura, E. Mekada, and N. Taniguchi (1996)
J. Biol. Chem. 271, 30858-30863
 |  Abstract »  |  Full Text »  |  PDF »

Characterization of the Mouse Epidermal Growth Factor Promoter and 5'-Flanking Region. ROLE FOR AN ATYPICAL TATA SEQUENCE.

S. E. Fenton, N. S. Groce, and D. C. Lee (1996)
J. Biol. Chem. 271, 30870-30878
 |  Abstract »  |  Full Text »  |  PDF »

Cysteines 153 and 154 of Transmembrane Transforming Growth Factor-alpha Are Palmitoylated and Mediate Cytoplasmic Protein Association.

L. Shum, C. W. Turck, and R. Derynck (1996)
J. Biol. Chem. 271, 28502-28508
 |  Abstract »  |  Full Text »  |  PDF »

The Epidermal Growth Factor Receptor Couples Transforming Growth Factor-alpha , Heparin-binding Epidermal Growth Factor-like Factor, and Amphiregulin to Neu, ErbB-3, and ErbB-4.

D. J. Riese II, E. D. Kim, K. Elenius, S. Buckley, M. Klagsbrun, G. D. Plowman, and D. F. Stern (1996)
J. Biol. Chem. 271, 20047-20052
 |  Abstract »  |  Full Text »  |  PDF »

COOH-terminal Extended Recombinant Amphiregulin with Bioactivity Comparable with Naturally Derived Growth Factor.

S. A. Thompson, A. Harris, D. Hoang, M. Ferrer, and G. R. Johnson (1996)
J. Biol. Chem. 271, 17927-17931
 |  Abstract »  |  Full Text »  |  PDF »

Insulin Regulates Heregulin Binding and ErbB3 Expression in Rat Hepatocytes.

R. S. Carver, M. X. Sliwkowski, S. Sitaric, and W. E. Russell (1996)
J. Biol. Chem. 271, 13491-13496
 |  Abstract »  |  Full Text »  |  PDF »

Epidermal Growth Factor-related Peptides Activate Distinct Subsets of ErbB Receptors and Differ in Their Biological Activities.

R. R. Beerli and N. E. Hynes (1996)
J. Biol. Chem. 271, 6071-6076
 |  Abstract »  |  Full Text »  |  PDF »

Amphiregulin in lung branching morphogenesis: interaction with heparan sulfate proteoglycan modulates cell proliferation.

L Schuger, G. Johnson, K Gilbride, G. Plowman, and R Mandel (1996)
Development 122, 1759-1767
 |  Abstract »  |  PDF »

HER4 Receptor Activation and Phosphorylation of Shc Proteins by Recombinant Heregulin-Fc Fusion Proteins.

J.-M. Culouscou, G. W. Carlton, and A. Aruffo (1995)
J. Biol. Chem. 270, 12857-12863
 |  Abstract »  |  Full Text »  |  PDF »

Epiregulin.

H. Toyoda, T. Komurasaki, D. Uchida, Y. Takayama, T. Isobe, T. Okuyama, and K. Hanada (1995)
J. Biol. Chem. 270, 7495-7500
 |  Abstract »  |  Full Text »  |  PDF »

TGF alpha can act as a chemoattractant to perioptic mesenchymal cells in developing mouse eyes.

L. Reneker, D. Silversides, K Patel, and P. Overbeek (1995)
Development 121, 1669-1680
 |  Abstract »  |  PDF »

The mouse waved-2 phenotype results from a point mutation in the EGF receptor tyrosine kinase..

N C Luetteke, H K Phillips, T H Qiu, N G Copeland, H S Earp, N A Jenkins, and D C Lee (1994)
Genes & Dev. 8, 399-413
 |  Abstract »  |  PDF »

The heparin-binding domain of heparin-binding EGF-like growth factor can target Pseudomonas exotoxin to kill cells exclusively through heparan sulfate proteoglycans.

E. Mesri, M Ono, R. Kreitman, M Klagsbrun, and I Pastan (1994)
J. Cell Sci. 107, 2599-2608
 |  Abstract »  |  PDF »

The murine cripto gene: expression during mesoderm induction and early heart morphogenesis.

R Dono, L Scalera, F Pacifico, D Acampora, M. Persico, and A Simeone (1993)
Development 118, 1157-1168
 |  Abstract »  |  PDF »

A genetic tool used to identify thioredoxin as a mediator of a growth inhibitory signal.

L. Deiss and A Kimchi (1991)
Science 252, 117-120
 |  Abstract »  |  PDF »

A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF.

S Higashiyama, J. Abraham, J Miller, J. Fiddes, and M Klagsbrun (1991)
Science 251, 936-939
 |  Abstract »  |  PDF »

Cloning and Biological Activity of Epigen, a Novel Member of the Epidermal Growth Factor Superfamily.

L. Strachan, J. G. Murison, R. L. Prestidge, M. A. Sleeman, J. D. Watson, and K. D. Kumble (2001)
J. Biol. Chem. 276, 18265-18271
 |  Abstract »  |  Full Text »  |  PDF »

Novel Betacellulin Derivatives. SEPARATION OF THE DIFFERENTIATION ACTIVITY FROM THE MITOGENIC ACTIVITY.

T. Itoh, M. Kondo, Y. Tanaka, M. Kobayashi, R. Sasada, K. Igarashi, M. Suenaga, N. Koyama, O. Nishimura, and M. Fujino (2001)
J. Biol. Chem. 276, 40698-40703
 |  Abstract »  |  Full Text »  |  PDF »

To Advertise   |   Find Products